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2npx
From Proteopedia
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(New page: 200px<br /><applet load="2npx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2npx, resolution 2.4Å" /> '''NADH BINDING SITE AND...) |
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| - | [[Image:2npx.jpg|left|200px]]<br /><applet load="2npx" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2npx, resolution 2.4Å" /> | ||
| - | '''NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE'''<br /> | ||
| - | == | + | ==NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE== |
| - | The structure of the complex between cofactor NADH and the enzyme NADH | + | <StructureSection load='2npx' size='340' side='right'caption='[[2npx]], [[Resolution|resolution]] 2.40Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2npx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NPX FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NADH_peroxidase NADH peroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.1 1.11.1.1] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2npx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2npx OCA], [https://pdbe.org/2npx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2npx RCSB], [https://www.ebi.ac.uk/pdbsum/2npx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2npx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/NAPE_ENTFA NAPE_ENTFA]] Peroxidase whose active site is a redox-active cysteine-sulfenic acid. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/np/2npx_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2npx ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The structure of the complex between cofactor NADH and the enzyme NADH peroxidase from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been determined by crystal soaking, X-ray data collection, model building of NADH and refinement at 0.24-nm resolution based on the known enzyme structure [Stehle, T., Ahmed, S. A., Claiborne, A. & Schulz, G. E. (1991) J. Mol. Biol. 221, 1325-1344]. Apart from NADH, the catalytic center of the enzyme contains FAD and a cysteine that shuttles between thiolate and sulfenic acid states. Unfortunately, this cysteine was irreversibly oxidized to a cysteine sulfonic acid in the established enzyme structure. Based on the geometry of the catalytic center, we discuss the stabilization of the oxidation-sensitive sulfenic acid and propose a reaction mechanism. | ||
| - | + | NADH binding site and catalysis of NADH peroxidase.,Stehle T, Claiborne A, Schulz GE Eur J Biochem. 1993 Jan 15;211(1-2):221-6. PMID:8425532<ref>PMID:8425532</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2npx" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[NADH peroxidase|NADH peroxidase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Enterococcus proteiformis thiercelin and jouhaud 1903]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: NADH peroxidase]] | ||
| + | [[Category: Claiborne, A]] | ||
| + | [[Category: Schulz, G E]] | ||
| + | [[Category: Stehle, T]] | ||
Current revision
NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE
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